ID TOC34_PEA Reviewed; 310 AA. AC Q41009; Q41029; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 14-DEC-2022, entry version 121. DE RecName: Full=Translocase of chloroplast 34; DE EC=3.6.5.-; DE AltName: Full=34 kDa chloroplast outer envelope protein; DE AltName: Full=GTP-binding protein IAP34; DE AltName: Full=GTP-binding protein OEP34; GN Name=TOC34; Synonyms=IAP34, OEP34; OS Pisum sativum (Garden pea). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=cv. Miranda; TISSUE=Leaf; RX PubMed=7757113; DOI=10.1046/j.1365-313x.1995.7030401.x; RA Seedorf M., Waegemann K., Soll J.; RT "A constituent of the chloroplast import complex represents a new type of RT GTP-binding protein."; RL Plant J. 7:401-411(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 119-139 AND 157-180. RX PubMed=7973656; DOI=10.1126/science.7973656; RA Kessler F., Blobel G., Patel H.V., Schnell D.J.; RT "Identification of two GTP-binding proteins in the chloroplast protein RT import machinery."; RL Science 266:1035-1039(1994). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-258 IN COMPLEX WITH GTP, RP HOMODIMERIZATION, AND MUTAGENESIS OF ARG-128. RX PubMed=11753431; DOI=10.1038/nsb744; RA Sun Y.-J., Forouhar F., Li Hm H.-M., Tu S.-L., Yeh Y.-H., Kao S., RA Shr H.-L., Chou C.-C., Chen C., Hsiao C.-D.; RT "Crystal structure of pea Toc34, a novel GTPase of the chloroplast protein RT translocon."; RL Nat. Struct. Biol. 9:95-100(2002). CC -!- FUNCTION: GTPase involved in protein precursor import into CC chloroplasts. Seems to recognize chloroplast-destined precursor CC proteins and regulate their presentation to the translocation channel CC through GTP hydrolysis. CC -!- SUBUNIT: Homodimer and monomer. Part of the TOC core complex that CC includes a protein for the specific recognition of transit peptides CC surrounded by a ring composed of four proteins forming translocation CC channels, and four to five GTP-binding proteins providing energy. This CC core complex can interact with components of the TIC complex to form a CC larger import complex. Chloroplastic protein precursor such as prSS CC (precursor of the RuBisCO small subunit) interacts with these CC complexes. The TOC complex contains a specific subset of polar lipids CC such as digalactosyldiacylglyceride (DGDG), phosphatidylcholine (PC) CC and phosphatidylglycerol (PG). TOC34 interacts at least with TOC75. CC {ECO:0000269|PubMed:11753431}. CC -!- INTERACTION: CC Q41009; Q41009: TOC34; NbExp=5; IntAct=EBI-638506, EBI-638506; CC Q41009; Q9MUK5: TOC64; NbExp=6; IntAct=EBI-638506, EBI-638487; CC Q41009; P48347: GRF10; Xeno; NbExp=2; IntAct=EBI-638506, EBI-1803304; CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family. CC TOC34 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z28341; CAA82196.1; -; mRNA. DR EMBL; L36856; AAC25785.1; -; mRNA. DR PIR; B55171; B55171. DR PDB; 1H65; X-ray; 2.00 A; A/B/C=1-258. DR PDB; 3BB1; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-266. DR PDBsum; 1H65; -. DR PDBsum; 3BB1; -. DR AlphaFoldDB; Q41009; -. DR SMR; Q41009; -. DR DIP; DIP-332N; -. DR IntAct; Q41009; 9. DR MINT; Q41009; -. DR TCDB; 3.A.9.1.1; the chloroplast envelope protein translocase (cept or tic-toc) family. DR EnsemblPlants; Psat3g083600.1; Psat3g083600.1.cds; Psat3g083600. DR Gramene; Psat3g083600.1; Psat3g083600.1.cds; Psat3g083600. DR BRENDA; 3.6.5.2; 4872. DR EvolutionaryTrace; Q41009; -. DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR006703; G_AIG1. DR InterPro; IPR045058; GIMA/IAN/Toc. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005688; Toc34. DR PANTHER; PTHR10903; GTPASE, IMAP FAMILY MEMBER-RELATED; 1. DR Pfam; PF04548; AIG1; 1. DR PIRSF; PIRSF038134; Toc34; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR00991; 3a0901s02IAP34; 1. DR PROSITE; PS51720; G_AIG1; 1. PE 1: Evidence at protein level; KW 3D-structure; Chloroplast; Direct protein sequencing; GTP-binding; KW Hydrolase; Membrane; Nucleotide-binding; Plastid; Plastid outer membrane; KW Protein transport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..310 FT /note="Translocase of chloroplast 34" FT /id="PRO_0000144793" FT TOPO_DOM 1..268 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 269..289 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 290..310 FT /note="Chloroplast intermembrane" FT /evidence="ECO:0000255" FT DOMAIN 37..260 FT /note="AIG1-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057" FT REGION 46..53 FT /note="G1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057" FT REGION 68..71 FT /note="Homodimerization" FT REGION 72..76 FT /note="G2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057" FT REGION 93..96 FT /note="G3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057" FT REGION 128..133 FT /note="Homodimerization" FT REGION 162..165 FT /note="G4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057" FT REGION 210..212 FT /note="G5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057" FT BINDING 49..54 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:11753431" FT BINDING 73 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:11753431" FT BINDING 210..211 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:11753431" FT MUTAGEN 128 FT /note="R->A: No dimerization and reduced GTPase activity." FT /evidence="ECO:0000269|PubMed:11753431" FT HELIX 12..16 FT /evidence="ECO:0007829|PDB:1H65" FT HELIX 19..34 FT /evidence="ECO:0007829|PDB:1H65" FT STRAND 39..47 FT /evidence="ECO:0007829|PDB:1H65" FT HELIX 52..60 FT /evidence="ECO:0007829|PDB:1H65" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:1H65" FT STRAND 78..84 FT /evidence="ECO:0007829|PDB:1H65" FT STRAND 87..93 FT /evidence="ECO:0007829|PDB:1H65" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:1H65" FT HELIX 105..114 FT /evidence="ECO:0007829|PDB:1H65" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:1H65" FT STRAND 122..130 FT /evidence="ECO:0007829|PDB:1H65" FT HELIX 136..149 FT /evidence="ECO:0007829|PDB:1H65" FT HELIX 151..156 FT /evidence="ECO:0007829|PDB:1H65" FT STRAND 157..162 FT /evidence="ECO:0007829|PDB:1H65" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:1H65" FT HELIX 174..192 FT /evidence="ECO:0007829|PDB:1H65" FT HELIX 200..202 FT /evidence="ECO:0007829|PDB:1H65" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:1H65" FT HELIX 231..243 FT /evidence="ECO:0007829|PDB:1H65" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:1H65" FT HELIX 254..258 FT /evidence="ECO:0007829|PDB:1H65" SQ SEQUENCE 310 AA; 34157 MW; 00D5E79735BF041F CRC64; MASQQQTVRE WSGINTFAPA TQTKLLELLG NLKQEDVNSL TILVMGKGGV GKSSTVNSII GERVVSISPF QSEGPRPVMV SRSRAGFTLN IIDTPGLIEG GYINDMALNI IKSFLLDKTI DVLLYVDRLD AYRVDNLDKL VAKAITDSFG KGIWNKAIVA LTHAQFSPPD GLPYDEFFSK RSEALLQVVR SGASLKKDAQ ASDIPVVLIE NSGRCNKNDS DEKVLPNGIA WIPHLVQTIT EVALNKSESI FVDKNLIDGP NPNQRGKLWI PLIFALQYLF LAKPIEALIR RDIATETKPA WETRDVGDRK //